Evidence map›Paper›PMID 19965770›Full record

ArticleNucleic acids research2010

A tale of two functions: enzymatic activity and translational repression by carboxyltransferase.

Glen Meades, Brian K Benson, Anne Grove, Grover L Waldrop

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 52 citations in OpenAlex.

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  6. ActivebioRxiv : the preprint server for biology · 2024
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  15. Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Glen MeadesDivision of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, LA 70803, USA.
Brian K Benson
Anne Grove
Grover L Waldrop
Louisiana State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetyl-CoA Carboxylase catalyzes the first committed step in fatty acid synthesis. Escherichia coli acetyl-CoA carboxylase is composed of biotin carboxylase, carboxyltransferase and biotin carboxyl carrier protein functions. The accA and accD genes that code for the alpha- and beta-subunits, respectively, are not in an operon, yet yield an alpha(2)beta(2) carboxyltransferase. Here, we report that carboxyltransferase regulates its own translation by binding the mRNA encoding its subunits. This interaction is mediated by a zinc finger on the beta-subunit; mutation of the four cysteines to alanine diminished nucleic acid binding and catalytic activity. Carboxyltransferase binds the coding regions of both subunit mRNAs and inhibits translation, an inhibition that is relieved by the substrate acetyl-CoA. mRNA binding reciprocally inhibits catalytic activity. Preferential binding of carboxyltransferase to RNA in situ was shown using fluorescence resonance energy transfer. We propose an unusual regulatory mechanism by which carboxyltransferase acts as a 'dimmer switch' to regulate protein production and catalytic activity, while sensing the metabolic state of the cell through acetyl-CoA concentration.

Indexed as

Gene Expression Regulation, BacterialGene Expression Regulation, EnzymologicProtein BiosynthesisAcetyl-CoA CarboxylaseBinding SitesCarboxyl and Carbamoyl TransferasesCatalysisDNAEscherichia coliEscherichia coli ProteinsProtein SubunitsRNA, MessengerZinc FingersAcetyl-CoA CarboxylaseCarboxyl and Carbamoyl TransferasesDNAEscherichia coli ProteinsProtein SubunitsRNA, Messenger

Identifiers

PMID19965770
PMCPMC2831308
OpenAlexW2156903017

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.